ID F4W4Q6_ACREC Unreviewed; 484 AA.
AC F4W4Q6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial {ECO:0000256|ARBA:ARBA00020294};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
DE AltName: Full=E2K {ECO:0000256|ARBA:ARBA00031331};
GN ORFNames=G5I_00380 {ECO:0000313|EMBL:EGI70822.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI70822.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 6/6.
CC {ECO:0000256|ARBA:ARBA00005145}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317}.
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DR EMBL; GL887547; EGI70822.1; -; Genomic_DNA.
DR RefSeq; XP_011051159.1; XM_011052857.1.
DR AlphaFoldDB; F4W4Q6; -.
DR STRING; 103372.F4W4Q6; -.
DR EnsemblMetazoa; XM_011052857.1; XP_011051159.1; LOC105144144.
DR GeneID; 105144144; -.
DR KEGG; aec:105144144; -.
DR eggNOG; KOG0559; Eukaryota.
DR InParanoid; F4W4Q6; -.
DR OrthoDB; 672at2759; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR006255; SucB.
DR NCBIfam; TIGR01347; sucB; 1.
DR PANTHER; PTHR43416:SF5; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Transferase {ECO:0000313|EMBL:EGI70822.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 81..155
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 161..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..219
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 52690 MW; 1CC26D1BC6097508 CRC64;
MAAMLSNCSR FAPRVITRSS VLRTEVARSL CSQGHTLIPV CIIHAEHVPN AKAPLCRKYK
ANYYWINQAR HIRSTSALWE IREVVVPAFA ESVNEGDVRW EKKVGDQVKE DEVLCEIETD
KTSVPVPSPG PGVIKELFFK DGDTVKPGQK LCTIDIGATG GAAPAEKTPQ PPAAAPAEKA
PKPASSPTSS APSVAPPLPR SAEPIPSPAT EPPSPQAPTA SMPVAAIKHA QSLESAKVQL
PPTDYTREII GTRTEQRVKM NRMRLRIAER LKDAQNTNAM LTTFNEIDMS RIIEFRKAHQ
ESFTKKYGIK LGFMSPFVMA SAYALKDQPV VNAVIDGTDI VYRDYVDISV AVATPKGLVV
PVLRSVENKN FAEIEIALAA LGEKARKGKI TIEDMDGGTF TISNGGVFGS MLGTPIINPP
QSAILGMHGV FDRPIAIKGE VKIRPMMYVA LTYDHRLIDG REAVMFLRKI KDAVEDPRII
LAGL
//
